A Potential Role for the Interaction of Wolbachia Surface Proteins with the Brugia malayi Glycolytic Enzymes and Cytoskeleton in Maintenance of Endosymbiosis
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{"title"=>"A Potential Role for the Interaction of Wolbachia Surface Proteins with the Brugia malayi Glycolytic Enzymes and Cytoskeleton in Maintenance of Endosymbiosis", "type"=>"journal", "authors"=>[{"first_name"=>"Elena", "last_name"=>"Melnikow", "scopus_author_id"=>"8911707300"}, {"first_name"=>"Shulin", "last_name"=>"Xu", "scopus_author_id"=>"41862759200"}, {"first_name"=>"Jing", "last_name"=>"Liu", "scopus_author_id"=>"56443664600"}, {"first_name"=>"Aaron J.", "last_name"=>"Bell", "scopus_author_id"=>"55941603600"}, {"first_name"=>"Elodie", "last_name"=>"Ghedin", "scopus_author_id"=>"55711597200"}, {"first_name"=>"Thomas R.", "last_name"=>"Unnasch", "scopus_author_id"=>"7005170465"}, {"first_name"=>"Sara", "last_name"=>"Lustigman", "scopus_author_id"=>"7003666182"}], "year"=>2013, "source"=>"PLoS Neglected Tropical Diseases", "identifiers"=>{"scopus"=>"2-s2.0-84876869486", "pmid"=>"23593519", "sgr"=>"84876869486", "doi"=>"10.1371/journal.pntd.0002151", "isbn"=>"1935-2735 (Electronic)\\r1935-2727 (Linking)", "issn"=>"19352735", "pui"=>"368819535"}, "id"=>"17d8c3df-6bf0-399f-8356-bf90549f9394", "abstract"=>"The human filarial parasite Brugia malayi harbors an endosymbiotic bacterium of the genus Wolbachia. The Wolbachia represent an attractive target for the control of filarial induced disease as elimination of the bacteria affects molting, reproduction and survival of the worms. The molecular basis for the symbiotic relationship between Wolbachia and their filarial hosts has yet to be elucidated. To identify proteins involved in this process, we focused on the Wolbachia surface proteins (WSPs), which are known to be involved in bacteria-host interactions in other bacterial systems. Two WSP-like proteins (wBm0152 and wBm0432) were localized to various host tissues of the B. malayi female adult worms and are present in the excretory/secretory products of the worms. We provide evidence that both of these proteins bind specifically to B. malayi crude protein extracts and to individual filarial proteins to create functional complexes. The wBm0432 interacts with several key enzymes involved in the host glycolytic pathway, including aldolase and enolase. The wBm0152 interacts with the host cytoskeletal proteins actin and tubulin. We also show these interactions in vitro and have verified that wBm0432 and B. malayi aldolase, as well as wBm0152 and B. malayi actin, co-localize to the vacuole surrounding Wolbachia. We propose that both WSP protein complexes interact with each other via the aldolase-actin link and/or via the possible interaction between the host's enolase and the cytoskeleton, and play a role in Wolbachia distribution during worm growth and embryogenesis.", "link"=>"http://www.mendeley.com/research/potential-role-interaction-wolbachia-surface-proteins-brugia-malayi-glycolytic-enzymes-cytoskeleton", "reader_count"=>55, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>19, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>16, "Student > Postgraduate"=>4, "Student > Master"=>3, "Other"=>2, "Student > Bachelor"=>3, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Researcher"=>19, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>16, "Student > Postgraduate"=>4, "Student > Master"=>3, "Other"=>2, "Student > Bachelor"=>3, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>4, "Engineering"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>41, "Medicine and Dentistry"=>2, "Chemistry"=>1, "Social Sciences"=>1, "Computer Science"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>1}, "Social Sciences"=>{"Social Sciences"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>41}, "Computer Science"=>{"Computer Science"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>4}}, "reader_count_by_country"=>{"United States"=>1, "Brazil"=>1, "Italy"=>1, "United Kingdom"=>2, "Portugal"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1015865"], "description"=>"<p>Plates were coated with 10 µg/ml of crude protein extract prepared from <i>B. malayi</i> (which contains the <i>w</i>Bm; solid line) or <i>A. viteae</i> (which lacks the endosymbiont; dashed line) and were then exposed to varying concentrations of purified recombinant His-tagged <i>w</i>Bm0152 (A), <i>w</i>Bm0432 (B), or <i>w</i>Bm0100 (C). The binding was detected using HRP-conjugated anti-His antibodies. OD: optical density. Data represent the mean absorbance at 450 nm ± S.D. of three independent experiments. The binding of recombinant WSP protein to <i>B. malayi</i> crude extracts was compared with its binding to <i>A. viteae</i> crude extract by a Student's two-tailed t test (<i>P</i><0.05).</p>", "links"=>[], "tags"=>["assay", "wsp-like", "proteins", "crude", "extracts", "parasitic", "filarial"], "article_id"=>675675, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.g001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ELISA_based_assay_to_test_for_possible_interaction_between_Wolbachia_WSP_like_proteins_and_crude_protein_extracts_of_parasitic_filarial_nematodes_/675675", "title"=>"ELISA-based assay to test for possible interaction between <i>Wolbachia</i> WSP-like proteins and crude protein extracts of parasitic filarial nematodes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:34:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015866"], "description"=>"<p>L-Photo-Leucine and L-Photo-Methionine metabolically labeled <i>B. malayi</i> worms were cross-linked for 20 minutes using UV followed by soluble protein crude extract preparation. The soluble extract was passed through an affinity column containing Protein G cross-linked to normal mouse IgG followed by affinity columns containing anti-<i>w</i>Bm0432 or anti-<i>w</i>Bm0152 antibodies cross-linked to Protein G. The corresponding protein eluates (6 µg/Lane) were run on a SDS-PAGE prior to Western blotting with (A) mouse anti-<i>w</i>Bm0432 specific antibodies (bands: ∼110 & 28 kDa) or (B) mouse anti-<i>w</i>Bm0152 specific antibodies (bands: ∼90 kDa and ∼120 kDa).</p>", "links"=>[], "tags"=>["complexes", "crude", "cross-linked", "metabolically", "labeled", "worm", "extract"], "article_id"=>675676, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.g002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Detection_of_Bm_w_Bm_protein_complexes_within_crude_cross_linked_metabolically_labeled_worm_extract_using_anti_w_Bm0432_or_anti_w_Bm0152_antibodies_/675676", "title"=>"Detection of <i>Bm</i>-<i>w</i>Bm protein complexes within crude cross-linked metabolically labeled worm extract using anti-<i>w</i>Bm0432 or anti-<i>w</i>Bm0152 antibodies.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:34:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015867"], "description"=>"<p>Enolase (Lane 1), aldolase iV (Lane 2), aldolase X (Lane 3), glyceraldehyde-3-phosphate dehydrogenase (Lane 4), triosephosphate isomerase (Lane 5), and recombinant His-tagged <i>w</i>Bm0432 (Lane 6), 3 µg each, were blotted onto nitrocellulose membrane and incubated for 3 h with binding buffer (<b>A</b>) or with 2 µg/ml of recombinant His-<i>w</i>Bm0432 (<b>B</b>). Binding was detected using HRP-conjugated mouse anti-His antibodies.</p>", "links"=>[], "tags"=>["wsp", "glycolytic", "enzymes"], "article_id"=>675677, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.g003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interaction_between_Wolbachia_WSP_w_Bm0432_and_glycolytic_enzymes_in_vitro_/675677", "title"=>"Interaction between <i>Wolbachia</i> WSP <i>w</i>Bm0432 and glycolytic enzymes <i>in vitro</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:34:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015868"], "description"=>"<p>(<b>A</b>) Aldolase overlay assay: Recombinant His-tagged <i>B. malayi</i> aldolase (3 µg) was blotted onto nitrocellulose membrane and individual strips were incubated for 3 h with: binding buffer (Lanes 1 & 2); 2 µg/ml of recombinant His-<i>w</i>Bm0432 (Lane 3); and 2 µg/ml His-<i>w</i>Bm0293 (Lane 4), an unrelated <i>Wolbachia</i> protein. Binding was detected using the following antibodies: mouse anti-His-<i>Bm</i>-aldolase (Lane 1); mouse anti-His-<i>w</i>Bm0432 (Lanes 2 & 3), and mouse anti-His-<i>w</i>Bm0293 (Lane 4), followed by HRP-conjugated secondary goat anti-mouse antibodies. (<b>B</b>) The <i>K<sub>d</sub></i> of <i>Wolbachia w</i>Bm0432 and aldolase interaction was determined by an overlay assay using recombinant His-tagged <i>B. malayi</i> aldolase (3 µg/Lane) blotted onto nitrocellulose membrane and incubation of the individual strips for 3 h with: 1, 2, 5 or 10 µg/ml of recombinant His-<i>w</i>Bm0432. Binding was detected using mouse anti-His-<i>w</i>Bm0432. (<b>C</b>) Actin overlay assay: Purified bovine actin (3 µg, Lane 1) and recombinant His- <i>w</i>Bm0152 (3 µg, Lanes 2–4) were blotted onto nitrocellulose membrane and individual strips were incubated for 3 h with: binding buffer (Lanes 1, 2, 4) or 2.5 µg/ml of bovine actin (Lane 3). Binding was detected using rabbit anti-actin (Lanes 1, 2, 3) or mouse anti-His-<i>w</i>Bm0152 (Lane 4) followed by HRP-conjugated goat anti-rabbit or goat anti-mouse antibodies, respectively. (<b>D</b>) The <i>K<sub>d</sub></i> of <i>Wolbachia w</i>Bm0152 and actin interaction was determined by ELISA-based assay. A plate coated with 20 µg/ml of His-<i>w</i>Bm0152 was exposed to varying concentrations of bovine actin. The binding was detected using rabbit Anti-actin polyclonal antibody followed by HRP-conjugated goat anti-rabbit IgG.</p>", "links"=>[], "tags"=>["wsps", "actin", "aldolase"], "article_id"=>675678, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.g004"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interaction_between_Wolbachia_WSPs_and_actin_or_B_malayi_aldolase_in_vitro_/675678", "title"=>"Interaction between <i>Wolbachia</i> WSPs and actin or <i>B. malayi</i> aldolase <i>in vitro</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:34:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015869"], "description"=>"<p>Cross sections of the hypodermal cord in female worms were probed with rabbit anti-<i>w</i>Bm0432 (A), mouse anti-<i>Bm</i>-aldolase (B), or both (C), followed by anti-rabbit gold (15 nm in A and 10 nm in C) or anti-mouse gold (18 nm in B and C). Cross sections of the hypodermal cord in female worms were probed with mouse anti-<i>w</i>Bm0152 (D), rabbit anti-actin (E), or both (F) followed by anti-mouse gold (15 nm in D and 18 nm in F) or anti-rabbit gold (15 nm in D and 10 nm in F). Bar: Panels A–F - 500 nm, inserts in Panels C and F - 100 nm. Note the proximity of <i>w</i>Bm0432 and aldolase (insert in C) as well as that of the <i>w</i>Bm0152 and actin within the <i>Wolbachia</i> vacuole (insert in F).</p>", "links"=>[], "tags"=>["wsp"], "article_id"=>675679, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.g005"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Co_localization_of_Wolbachia_WSP_protein_w_Bm0432_with_Bm_aldolase_and_w_Bm0152_with_Bm_actin_/675679", "title"=>"Co-localization of <i>Wolbachia</i> WSP protein <i>w</i>Bm0432 with <i>Bm</i>-aldolase and <i>w</i>Bm0152 with <i>Bm</i>-actin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:34:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015870"], "description"=>"<p>Actin (Lane 1) or recombinant His-tagged <i>Bm</i>-aldolase (3 µg) (Lanes 2 and 3) were blotted onto nitrocellulose membrane and the individual strips were incubated for 3 h with: binding buffer (Lanes 1 and 2) or 2.5 µg/ml of bovine actin (Lane 3). Binding was detected using goat anti-actin followed by HRP-conjugated anti-goat antibodies.</p>", "links"=>[], "tags"=>["assay"], "article_id"=>675680, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.g006"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overlay_assay_to_prove_the_interaction_between_Bm_aldolase_and_actin_/675680", "title"=>"Overlay assay to prove the interaction between <i>Bm</i>-aldolase and actin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:34:40"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015872"], "description"=>"<p>The complex of <i>w</i>Bm0432 with the GE proteins is potentially associated with the complex of <i>w</i>Bm0152/cytoskeletal proteins via aldolase and/or enolase.</p>", "links"=>[], "tags"=>["Infectious diseases"], "article_id"=>675682, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.g007"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_model_for_Bm_w_Bm_interactions_/675682", "title"=>"The model for <i>Bm</i>-<i>w</i>Bm interactions.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:34:42"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015873"], "description"=>"<p>Sequences of gene specific primers used for cloning.</p>", "links"=>[], "tags"=>["primers"], "article_id"=>675683, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.t001"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequences_of_gene_specific_primers_used_for_cloning_/675683", "title"=>"Sequences of gene specific primers used for cloning.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-04-04 01:34:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015874"], "description"=>"a<p>Photo-activated crosslinked adult female <i>B. malayi</i> extracts complexes were eluted from affinity columns containing anti-<i>w</i>Bm0432 or anti-<i>w</i>Bm0152 antibodies bound to protein G.</p>**<p>: members of the glycolytic enzymes.</p>*<p>: cytoskeleton complexes.</p>", "links"=>[], "tags"=>["wsp", "complexes", "lc-ms"], "article_id"=>675684, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.t003"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Composition_of_the_B_malayi_Wolbachia_WSP_protein_complexes_identified_by_LC_MS_analyses_/675684", "title"=>"Composition of the <i>B. malayi</i> – <i>Wolbachia</i> WSP protein complexes identified by LC-MS analyses.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-04-04 01:34:44"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015875"], "description"=>"a<p>BLAST searches were used to identify <i>O. cuniculus</i> GEs orthologs in <i>B. malayi</i>.</p>", "links"=>[], "tags"=>["conserved"], "article_id"=>675685, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.t002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GEs_are_conserved_between_O_cuniculus_and_B_malayi_/675685", "title"=>"GEs are conserved between <i>O. cuniculus</i> and <i>B. malayi</i>.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-04-04 01:34:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/1015876", "https://ndownloader.figshare.com/files/1015877"], "description"=>"<div><p>The human filarial parasite <i>Brugia malayi</i> harbors an endosymbiotic bacterium of the genus <i>Wolbachia</i>. The <i>Wolbachia</i> represent an attractive target for the control of filarial induced disease as elimination of the bacteria affects molting, reproduction and survival of the worms. The molecular basis for the symbiotic relationship between <i>Wolbachia</i> and their filarial hosts has yet to be elucidated. To identify proteins involved in this process, we focused on the <i>Wolbachia</i> surface proteins (WSPs), which are known to be involved in bacteria-host interactions in other bacterial systems. Two WSP-like proteins (<i>w</i>Bm0152 and <i>w</i>Bm0432) were localized to various host tissues of the <i>B. malayi</i> female adult worms and are present in the excretory/secretory products of the worms. We provide evidence that both of these proteins bind specifically to <i>B. malayi</i> crude protein extracts and to individual filarial proteins to create functional complexes. The <i>w</i>Bm0432 interacts with several key enzymes involved in the host glycolytic pathway, including aldolase and enolase. The <i>w</i>Bm0152 interacts with the host cytoskeletal proteins actin and tubulin. We also show these interactions <i>in vitro</i> and have verified that <i>w</i>Bm0432 and <i>B. malayi</i> aldolase, as well as <i>w</i>Bm0152 and <i>B. malayi</i> actin, co-localize to the vacuole surrounding <i>Wolbachia</i>. We propose that both WSP protein complexes interact with each other via the aldolase-actin link and/or via the possible interaction between the host's enolase and the cytoskeleton, and play a role in <i>Wolbachia</i> distribution during worm growth and embryogenesis.</p> </div>", "links"=>[], "tags"=>["proteins", "glycolytic", "enzymes", "cytoskeleton", "endosymbiosis"], "article_id"=>675686, "categories"=>["Infectious Diseases"], "users"=>["Elena Melnikow", "Shulin Xu", "Jing Liu", "Aaron J. Bell", "Elodie Ghedin", "Thomas R. Unnasch", "Sara Lustigman"], "doi"=>["https://dx.doi.org/10.1371/journal.pntd.0002151.s001", "https://dx.doi.org/10.1371/journal.pntd.0002151.s002"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/A_Potential_Role_for_the_Interaction_of_Wolbachia_Surface_Proteins_with_the_Brugia_malayi_Glycolytic_Enzymes_and_Cytoskeleton_in_Maintenance_of_Endosymbiosis/675686", "title"=>"A Potential Role for the Interaction of <i>Wolbachia</i> Surface Proteins with the <i>Brugia malayi</i> Glycolytic Enzymes and Cytoskeleton in Maintenance of Endosymbiosis", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-04-04 01:34:46"}

PMC Usage Stats | Further Information

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Relative Metric

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